1lhs: Difference between revisions

Revision as of 20:56, 2 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1lhs.png

Template:STRUCTURE 1lhs

LOGGERHEAD SEA TURTLE MYOGLOBIN (AQUO-MET)LOGGERHEAD SEA TURTLE MYOGLOBIN (AQUO-MET)

Template:ABSTRACT PUBMED 7714901

About this StructureAbout this Structure

1LHS is a Single protein structure of sequence from Caretta caretta. Full crystallographic information is available from OCA.

ReferenceReference

Reptile heme protein structure: X-ray crystallographic study of the aquo-met and cyano-met derivatives of the loggerhead sea turtle (Caretta caretta) myoglobin at 2.0 A resolution., Nardini M, Tarricone C, Rizzi M, Lania A, Desideri A, De Sanctis G, Coletta M, Petruzzelli R, Ascenzi P, Coda A, et al., J Mol Biol. 1995 Mar 31;247(3):459-65. PMID:7714901

Page seeded by OCA on Wed Jul 2 20:56:35 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1lhs.jpg|left|200px]]
+{{Seed}}
+[[Image:1lhs.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1lhs|  PDB=1lhs  |  SCENE=  }}
-'''LOGGERHEAD SEA TURTLE MYOGLOBIN (AQUO-MET)'''
+===LOGGERHEAD SEA TURTLE MYOGLOBIN (AQUO-MET)===
-==Overview==
+<!--
-The X-ray crystal structures of the aquo-met and cyano-met derivatives of the loggerhead sea turtle (Caretta caretta) myoglobin have been determined at 2.0 A resolution (R = 0.182, and 0.178, respectively). The results here reported, representing the first reptile globin solved by X-ray crystallography, have been analyzed in parallel with data for related monomeric hemoproteins, and indicate a strong overall structural similarity between the loggerhead sea turtle and mammalian myoglobins, reflected by the 63% amino acid identity of their primary structures. The root-mean-square deviation between the entire polypeptide backbones of loggerhead sea turtle and sperm whale myoglobins, after structure superposition, is 0.83 A. Upon cyanide binding to the protein distal site, the iron-bound water molecule present in the aquo-met form is displaced by the incoming ligand. Cyanide is oriented towards the inner part of the heme distal site forming a Fe-C-N angle of 133 degrees.
+The line below this paragraph, {{ABSTRACT_PUBMED_7714901}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 7714901 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_7714901}}
 ==About this Structure==
@@ Line 33: / Line 37: @@
 [[Category: Tarricone, C.]]
 [[Category: Oxygen storage]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 23:55:57 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul  2 20:56:35 2008''